EUTT_SALTY
ID EUTT_SALTY Reviewed; 267 AA.
AC Q9ZFV4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Corrinoid adenosyltransferase EutT {ECO:0000305};
DE AltName: Full=ATP:co(I)rrinoid adenosyltransferase {ECO:0000303|PubMed:16636051};
DE Short=ACAT {ECO:0000303|PubMed:24336938};
DE AltName: Full=Cob(II)alamin adenosyltransferase EutT {ECO:0000303|PubMed:15516577};
DE AltName: Full=Ethanolamine utilization cobalamin adenosyltransferase;
DE AltName: Full=Ethanolamine utilization corrinoid adenosyltransferase;
DE AltName: Full=EutT adenosyltransferase {ECO:0000303|PubMed:15516577};
GN Name=eutT {ECO:0000303|PubMed:10464203}; OrderedLocusNames=STM2467;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA Roof D.M., Roth J.R.;
RT "Ethanolamine utilization in Salmonella typhimurium.";
RL J. Bacteriol. 170:3855-3863(1988).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=15516577; DOI=10.1128/jb.186.22.7635-7644.2004;
RA Sheppard D.E., Penrod J.T., Bobik T., Kofoid E., Roth J.R.;
RT "Evidence that a B12-adenosyl transferase is encoded within the
RT ethanolamine operon of Salmonella enterica.";
RL J. Bacteriol. 186:7635-7644(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-79; CYS-80 AND
RP CYS-83.
RC STRAIN=LT2;
RX PubMed=16636051; DOI=10.1074/jbc.m603069200;
RA Buan N.R., Escalante-Semerena J.C.;
RT "Purification and initial biochemical characterization of ATP:Cob(I)alamin
RT adenosyltransferase (EutT) enzyme of Salmonella enterica.";
RL J. Biol. Chem. 281:16971-16977(2006).
RN [7]
RP FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF HIS-67; HIS-75; CYS-79;
RP CYS-80 AND CYS-83.
RC STRAIN=LT2;
RX PubMed=24336938; DOI=10.1128/jb.01304-13;
RA Moore T.C., Mera P.E., Escalante-Semerena J.C.;
RT "The EutT enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin
RT adenosyltransferase metalloprotein that requires ferrous ions for maximal
RT activity.";
RL J. Bacteriol. 196:903-910(2014).
RN [8]
RP COFACTOR, AND MUTAGENESIS OF HIS-67; HIS-75; CYS-79; CYS-80 AND CYS-83.
RC STRAIN=LT2;
RX PubMed=28045498; DOI=10.1021/acs.biochem.6b00750;
RA Pallares I.G., Moore T.C., Escalante-Semerena J.C., Brunold T.C.;
RT "Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella
RT enterica: Evidence of a Tetrahedrally Coordinated Divalent Transition Metal
RT Cofactor with Cysteine Ligation.";
RL Biochemistry 56:364-375(2017).
RN [9]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=29531136; DOI=10.1128/iai.00172-18;
RA Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT enterica and Listeria monocytogenes during Macrophage Infection.";
RL Infect. Immun. 86:0-0(2018).
CC -!- FUNCTION: Converts cyanocobalamin (CN-B12) to adenosylcobalamin
CC (AdoCbl), the inducer of the eut operon (PubMed:15516577,
CC PubMed:16636051, PubMed:24336938). Is not active on cobinamide nor
CC other intermediates in the adenosylcobalamin synthetic pathway. Allows
CC full induction of the eut operon (PubMed:15516577). Can use ADP, CTP
CC and dATP in place of ATP, and cobinamide in place of cobalamin, none
CC are as efficiently used as ATP and cobalamin (PubMed:16636051).
CC {ECO:0000269|PubMed:15516577, ECO:0000269|PubMed:16636051,
CC ECO:0000269|PubMed:24336938}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on
CC cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078).
CC EA enhances bacterial survival in macrophages in a concentration-
CC dependent manner, suggesting it is an important nutrient during
CC infection (PubMed:29531136). {ECO:0000269|PubMed:29531136,
CC ECO:0000269|PubMed:3045078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)inamide + 2 H2O + reduced [electron-transfer
CC flavoprotein] = 2 adenosylcob(III)inamide + 2 diphosphate + 3 H(+) +
CC oxidized [electron-transfer flavoprotein] + 2 phosphate;
CC Xref=Rhea:RHEA:66824, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:2480, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:141013;
CC Evidence={ECO:0000269|PubMed:16636051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cob(I)alamin-[corrinoid adenosyltransferase] =
CC adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] +
CC triphosphate; Xref=Rhea:RHEA:56796, Rhea:RHEA-COMP:14743, Rhea:RHEA-
CC COMP:14744, ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60488, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000305|PubMed:15516577};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:16636051, ECO:0000269|PubMed:24336938,
CC ECO:0000269|PubMed:28045498};
CC Note=Binds 1 divalent metal cation ion per homodimer with both subunits
CC providing Cys ligands; Fe(2+) gives most activity and is possibly the
CC physiological cofactor, followed by Zn(2+) and Co(2+) (PubMed:24336938,
CC PubMed:28045498). Activity stimulated by Mn(2+) (PubMed:16636051).
CC {ECO:0000269|PubMed:16636051, ECO:0000269|PubMed:24336938,
CC ECO:0000269|PubMed:28045498};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for ATP {ECO:0000269|PubMed:16636051};
CC KM=4.1 uM for cob(I)alamin {ECO:0000269|PubMed:16636051};
CC Note=kcat is 0.03 sec(-1). {ECO:0000269|PubMed:16636051};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:16636051};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24336938}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000305}.
CC -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12). {ECO:0000269|PubMed:3045078}.
CC -!- DISRUPTION PHENOTYPE: A quadruple eutP-eutQ-eutT-eutD deletion is not
CC impaired for aerobic growth on ethanolamine (EA) supplemented with
CC cobalamin (vitamin B12) (PubMed:10464203). Can grow on EA as sole
CC carbon source when AdoB12 is supplied; double cobA-eutT mutants do not
CC grow with CN-B12 as a nitrogen source (PubMed:15516577). A non-polar
CC deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at
CC pH 8.5, no change in acetaldehyde release on EA plus vitamin B12
CC (PubMed:16585748). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:15516577, ECO:0000269|PubMed:16585748}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC EutT subfamily. {ECO:0000305}.
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DR EMBL; AF093749; AAC78114.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21361.1; -; Genomic_DNA.
DR RefSeq; NP_461402.1; NC_003197.2.
DR RefSeq; WP_000997656.1; NC_003197.2.
DR AlphaFoldDB; Q9ZFV4; -.
DR SMR; Q9ZFV4; -.
DR STRING; 99287.STM2467; -.
DR PaxDb; Q9ZFV4; -.
DR EnsemblBacteria; AAL21361; AAL21361; STM2467.
DR GeneID; 1253989; -.
DR KEGG; stm:STM2467; -.
DR PATRIC; fig|99287.12.peg.2605; -.
DR HOGENOM; CLU_093470_1_0_6; -.
DR OMA; ACCELCH; -.
DR PhylomeDB; Q9ZFV4; -.
DR BioCyc; MetaCyc:STM2467-MON; -.
DR BioCyc; SENT99287:STM2467-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1200.10; -; 1.
DR InterPro; IPR009194; AdoTrfase_EutT.
DR InterPro; IPR016030; CblAdoTrfase-like.
DR InterPro; IPR036451; CblAdoTrfase-like_sf.
DR Pfam; PF01923; Cob_adeno_trans; 1.
DR PIRSF; PIRSF012294; ATR_EutT; 1.
DR SUPFAM; SSF89028; SSF89028; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Bacterial microcompartment; Iron; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Corrinoid adenosyltransferase EutT"
FT /id="PRO_0000087101"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000305|PubMed:16636051,
FT ECO:0000305|PubMed:24336938, ECO:0000305|PubMed:28045498"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000305|PubMed:16636051,
FT ECO:0000305|PubMed:24336938, ECO:0000305|PubMed:28045498"
FT MUTAGEN 67
FT /note="H->A: Reduces metal content of enzyme, does not
FT complement deletion. No binding of Co(2+)."
FT /evidence="ECO:0000269|PubMed:24336938,
FT ECO:0000269|PubMed:28045498"
FT MUTAGEN 75
FT /note="H->A: No effect in vivo or in vitro. No binding of
FT Co(2+)."
FT /evidence="ECO:0000269|PubMed:24336938,
FT ECO:0000269|PubMed:28045498"
FT MUTAGEN 79
FT /note="C->A: Does not complement deletion, 20% activity in
FT vitro. Reduces metal content of enzyme, complements a
FT deletion."
FT /evidence="ECO:0000269|PubMed:16636051,
FT ECO:0000269|PubMed:24336938, ECO:0000269|PubMed:28045498"
FT MUTAGEN 80
FT /note="C->A: Does not complement deletion, 0.6% activity in
FT vitro. No metal cofactor."
FT /evidence="ECO:0000269|PubMed:16636051,
FT ECO:0000269|PubMed:24336938, ECO:0000269|PubMed:28045498"
FT MUTAGEN 83
FT /note="C->A: Does not complement deletion, 1.2% activity in
FT vitro. No metal cofactor."
FT /evidence="ECO:0000269|PubMed:16636051,
FT ECO:0000269|PubMed:24336938, ECO:0000269|PubMed:28045498"
SQ SEQUENCE 267 AA; 30239 MW; 9502A28FDB4DC9E4 CRC64;
MNDFITETWL RANHTLSEGS EIHLPADARL TPSARELLES RRLRIKFLDP QGRLFVDDDE
QQPQPVHGLT SSDTHPQACC ELCRQPVVKK PDTLTHLTAD KMVAKSDPRL GFRAALDSAI
ALTVWLQIEL AEPWQPWLFD IRSRLGNIMR ADAIDEPLAA QSIVGLNEDE LHRLSHQPLR
YLDHDHLVPE ASHGRDAALL NLLRTKVRET ETLAAQVFIT RSFEVLRPDI LQALNRLSST
VYVMMILSVA KHPLTVAQIQ QRLGEKP
